3KLL

Crystal structure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180-maltose complex

3KLL の概要

• エントリーDOI: 10.2210/pdb3kll/pdb
• 関連するPDBエントリー: 3HQ3 3HZ3 3KLK
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Glucansucrase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: glucansucrase-maltose complex, multidomain protein, glycosyltransferase, transferase
• 由来する生物種: Lactobacillus reuteri
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 119544.98

構造登録者

Vujicic-Zagar, A.,Pijning, T.,Kralj, S.,Eeuwema, W.,Dijkhuizen, L.,Dijkstra, B.W. (登録日: 2009-11-08, 公開日: 2010-11-03, 最終更新日: 2024-11-06)

主引用文献

Vujicic-Zagar, A.,Pijning, T.,Kralj, S.,Lopez, C.A.,Eeuwema, W.,Dijkhuizen, L.,Dijkstra, B.W.
Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes
Proc.Natl.Acad.Sci.USA, 107:21406-21411, 2010

PubMed Abstract: Glucansucrases are large enzymes belonging to glycoside hydrolase family 70, which catalyze the cleavage of sucrose into fructose and glucose, with the concomitant transfer of the glucose residue to a growing α-glucan polymer. Among others, plaque-forming oral bacteria secrete these enzymes to produce α-glucans, which facilitate the adhesion of the bacteria to the tooth enamel. We determined the crystal structure of a fully active, 1,031-residue fragment encompassing the catalytic and C-terminal domains of GTF180 from Lactobacillus reuteri 180, both in the native state, and in complexes with sucrose and maltose. These structures show that the enzyme has an α-amylase-like (β/α)(8)-barrel catalytic domain that is circularly permuted compared to the catalytic domains of members of glycoside hydrolase families 13 and 77, which belong to the same GH-H superfamily. In contrast to previous suggestions, the enzyme has only one active site and one nucleophilic residue. Surprisingly, in GTF180 the peptide chain follows a "U"-path, such that four of the five domains are made up from discontiguous N- and C-terminal stretches of the peptide chain. Finally, the structures give insight into the factors that determine the different linkage types in the polymeric product.

PubMed: 21118988
DOI: 10.1073/pnas.1007531107

実験手法

X-RAY DIFFRACTION (2 Å)